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SUMMARY:The characterization and crystallization of the TBR1 T-box domain 
 in the presence and absence of the T-box Binding Element
DTSTART;VALUE=DATE-TIME:20210322T144000Z
DTEND;VALUE=DATE-TIME:20210322T150000Z
DTSTAMP;VALUE=DATE-TIME:20260714T160639Z
UID:indico-contribution-6956@events.saip.org.za
DESCRIPTION:Speakers: Riyaadh Mayet (University of the Witwatersrand)\nTBR
 1 is a neuron-specific transcription factor involved in multiple aspects o
 f cortical development\,and has recently emerged as a master regulator of 
 genes implicated in Autism Spectrum Disorder (ASD).It is thus possible tha
 t aberrant molecular interactions with TBR1 could underlie the altered neu
 ro-molecular networks observed in Autism.\n\nCurrently there is no solved 
 structure available of the TBR1 TBOX domain. In this study\, we aim to obt
 ain crystal structures of the TBR1 T-box domain in both the presence and a
 bsence of the T-box binding element\, with the hope of elucidating its DNA
 -binding mechanism. The structure may be solved by molecular replacement u
 sing TBX21. This will shed more light on how TBR1 regulates ASD-related ge
 nes and could explain how aberrant molecular interactions influence neurod
 evelopmental disorders.\n\nPreliminary structural characterization has bee
 n made by monitoring intrinsic tryptophan fluorescence and has revealed th
 at the protein is properly folded. The DNA-binding function has been confi
 rmed using an electrophoretic mobility shift assay. The DNA-binding proper
 ties were quantitatively assessed using fluorescence anisotropy and reveal
 ed a dissociation constant of 320 nM. Since the TBR1 T-box has been succes
 sfully characterized\, it is ready for crystal trials.\n\nhttps://events.s
 aip.org.za/event/213/contributions/6956/
LOCATION:Zoom Conference
URL:https://events.saip.org.za/event/213/contributions/6956/
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